1rxl

<StructureSection load='1rxl' size='340' side='right'caption='[[1rxl]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1rxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RXL FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sdd|1sdd]], [[1ut2|1ut2]], [[1ut1|1ut1]], [[1usq|1usq]], [[1usz|1usz]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">afae3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

[[https://www.uniprot.org/uniprot/AFAE3_ECOLX AFAE3_ECOLX]] Hemagglutinins of uropathogenic E.coli mediate adherence to the upper urinary tract. These adhesins bind to the Dr blood group antigen and also agglutinate human erythrocytes in the presence of D-mannose (mannose-resistant hemagglutination (MRHA)).

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== Publication Abstract from PubMed ==

Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.

An atomic resolution model for assembly, architecture, and function of the Dr adhesins.,Anderson KL, Billington J, Pettigrew D, Cota E, Simpson P, Roversi P, Chen HA, Urvil P, du Merle L, Barlow PN, Medof ME, Smith RA, Nowicki B, Le Bouguenec C, Lea SM, Matthews S Mol Cell. 2004 Aug 27;15(4):647-57. PMID:15327779<ref>PMID:15327779</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rxl" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Anderson, K L]]

[[Category: Barlow, P N]]

[[Category: Billington, J]]

[[Category: Bouguenec, C Le]]

[[Category: Chen, H A]]

[[Category: Cota, E]]

[[Category: Lea, S M]]

[[Category: Matthews, S]]

[[Category: Medof, M E]]

[[Category: Merle, L du]]

[[Category: Nowicki, B]]

[[Category: Pettigrew, D]]

[[Category: Roversi, P]]

[[Category: Simpson, P]]

[[Category: Smith, R A]]

[[Category: Urvil, P]]

[[Category: Afae]]

[[Category: Upec]]